ID A0A2N5X0M1_9ACTN Unreviewed; 447 AA.
AC A0A2N5X0M1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
DE Flags: Fragment;
GN ORFNames=C0036_21020 {ECO:0000313|EMBL:PLW68034.1};
OS Streptomyces sp. DJ.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2067551 {ECO:0000313|EMBL:PLW68034.1, ECO:0000313|Proteomes:UP000235150};
RN [1] {ECO:0000313|EMBL:PLW68034.1, ECO:0000313|Proteomes:UP000235150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ {ECO:0000313|EMBL:PLW68034.1,
RC ECO:0000313|Proteomes:UP000235150};
RA Ke Y., Yu G., Ye J., Yuan X.;
RT "Genome of Streptomyces sp. DJ strain.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW68034.1}.
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DR EMBL; PKSK01001596; PLW68034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5X0M1; -.
DR Proteomes; UP000235150; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000235150}.
FT DOMAIN 4..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 447
FT /evidence="ECO:0000313|EMBL:PLW68034.1"
SQ SEQUENCE 447 AA; 46620 MW; DCB07E42332F17B5 CRC64;
MTTLFDTVLV ANRGEIAVRV VRTLRRLGIR SVAVYSDADA RARHVAEADT AVRIGPPAAS
GSYLSAERIV EAALRTGAQA VHPGYGFLAE NAAFARACAD AGLVFVGPPA SAVELMGDKI
RAKETVKAAG VPVVPGSSGS GLTDAQLVAA AEEIGVPVLL KPSAGGGGKG MRLVRDLAAL
PEEIAAARRE ARGSFGDDTL LLERWIDRPR HIEIQVLADA HGGVIHLGER ECSLQRRHQK
LIEEAPSPLL DAATRAAMGE AAVRAARSCG YTGAGTVEFI VPGDDPSSYF FMEMNTRLQV
EHPVTEMVTG LDLVEWQIRT AAGEHLPLAQ EDVALDGHAV EARICAETVS VTAGSPAFLP
SGGSVLLLRE PDGEGVRTDS GLAQGTEVGS LYDPMLSKVI AHGPDRATAL RRLRAALAGT
VTLGVPTNAG FLRRLLADPD VVAGAAA
//
